ID S0JH46_9FIRM Unreviewed; 347 AA.
AC S0JH46;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=N-acetylmuramoyl-L-alanine amidase {ECO:0000256|ARBA:ARBA00011901};
DE EC=3.5.1.28 {ECO:0000256|ARBA:ARBA00011901};
GN ORFNames=C805_01275 {ECO:0000313|EMBL:EOT27168.1};
OS Eubacterium sp. 14-2.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Eubacterium.
OX NCBI_TaxID=1235790 {ECO:0000313|EMBL:EOT27168.1, ECO:0000313|Proteomes:UP000014176};
RN [1] {ECO:0000313|EMBL:EOT27168.1, ECO:0000313|Proteomes:UP000014176}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=14-2 {ECO:0000313|EMBL:EOT27168.1,
RC ECO:0000313|Proteomes:UP000014176};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Xavier R., Elson C., Duck W., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Eubacterium bacterium 14-2.";
RL Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolyzes the link between N-acetylmuramoyl residues and L-
CC amino acid residues in certain cell-wall glycopeptides.; EC=3.5.1.28;
CC Evidence={ECO:0000256|ARBA:ARBA00001561};
CC -!- SIMILARITY: Belongs to the N-acetylmuramoyl-L-alanine amidase 2 family.
CC {ECO:0000256|ARBA:ARBA00007553}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EOT27168.1}.
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DR EMBL; ASSS01000005; EOT27168.1; -; Genomic_DNA.
DR RefSeq; WP_016214330.1; NZ_KE159567.1.
DR AlphaFoldDB; S0JH46; -.
DR STRING; 1235790.C805_01275; -.
DR PATRIC; fig|1235790.3.peg.1347; -.
DR eggNOG; COG5632; Bacteria.
DR HOGENOM; CLU_047675_1_1_9; -.
DR OrthoDB; 9794294at2; -.
DR Proteomes; UP000014176; Unassembled WGS sequence.
DR GO; GO:0008745; F:N-acetylmuramoyl-L-alanine amidase activity; IEA:InterPro.
DR GO; GO:0030420; P:establishment of competence for transformation; IEA:UniProtKB-KW.
DR GO; GO:0009253; P:peptidoglycan catabolic process; IEA:InterPro.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR CDD; cd06583; PGRP; 1.
DR Gene3D; 3.40.80.10; Peptidoglycan recognition protein-like; 1.
DR InterPro; IPR036505; Amidase/PGRP_sf.
DR InterPro; IPR002502; Amidase_domain.
DR PANTHER; PTHR30417; N-ACETYLMURAMOYL-L-ALANINE AMIDASE AMID; 1.
DR PANTHER; PTHR30417:SF11; N-ACETYLMURAMOYL-L-ALANINE AMIDASE XLYA; 1.
DR Pfam; PF01510; Amidase_2; 1.
DR SMART; SM00644; Ami_2; 1.
DR SUPFAM; SSF55846; N-acetylmuramoyl-L-alanine amidase-like; 1.
PE 3: Inferred from homology;
KW Competence {ECO:0000256|ARBA:ARBA00023287};
KW Reference proteome {ECO:0000313|Proteomes:UP000014176};
KW Sporulation {ECO:0000256|ARBA:ARBA00022969}.
FT DOMAIN 9..151
FT /note="N-acetylmuramoyl-L-alanine amidase"
FT /evidence="ECO:0000259|SMART:SM00644"
SQ SEQUENCE 347 AA; 38975 MW; D17C49C54DD27B81 CRC64;
MTINRDYVST QNTYENENRP KYIVIHETDN YAKGADARRH ASAQAAGHLS TSVHYYAGSD
GVCQAAEHKD GTFSIGVEYN ASHAVKDADN RNTINIEICV NSDGDYGKAR ENAIALVREL
LRDTDIPVER VIRHFDARGK YCPRKMMDSP GLWTDFQNQI GRKEPEDDSG TSQGEHEPAE
IWYRVGSGWK NGICQNQTGA YHNREFAVAD CRPGQYVYDE EGNIVYSGDD RNGQDFTYTQ
KQFIRDVQKT TGSVPDGIAG DETIGNTLTV SRSDNKYHPV VTSLERRMKA LNYYRGAIEE
DSGERPHFGK GMEEAVNSYQ KKVLGYKNPD GEITGKKKTW ESLLGML
//
